Lmfa07050031

Lmfa07050031 is a lipid of Fatty Acyls (FA) class. The involved functions are known as Pigment and Polymerization. The related lipids are Propionate.

Cross Reference

Introduction

To understand associated biological information of Lmfa07050031, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with Lmfa07050031

MeSH term MeSH ID Detail
Diabetes Mellitus D003920 90 associated lipids
Adenocarcinoma D000230 166 associated lipids
Reperfusion Injury D015427 65 associated lipids
Diabetes Mellitus, Type 2 D003924 87 associated lipids
Fatty Liver D005234 48 associated lipids
Ketosis D007662 13 associated lipids
Body Weight D001835 333 associated lipids
Heart Failure D006333 36 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Hypothyroidism D007037 32 associated lipids
Per page 10 20 50 | Total 27

PubChem Associated disorders and diseases

What pathways are associated with Lmfa07050031

There are no associated biomedical information in the current reference collection.

PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

What functions are associated with Lmfa07050031?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with Lmfa07050031?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
Loading... please refresh the page if content is not showing up.

What genes are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

What common seen animal models are associated with Lmfa07050031?

There are no associated biomedical information in the current reference collection.

NCBI Entrez Crosslinks

All references with Lmfa07050031

Download all related citations
Per page 10 20 50 100 | Total 787
Authors Title Published Journal PubMed Link
Wahle KW et al. Biosynthesis of branched-chain fatty acids by preparations from bovine adipose tissue [proceedings]. 1978 Biochem. Soc. Trans. pmid:744376
Cook GA and Weakley LJ Effects of starvation on the carnitine palmitoyltransferase of hepatic peroxisomes. 1990 Biochem. Soc. Trans. pmid:2083787
Mynatt RL and Cook GA Modulation of the malonyl-CoA sensitivity of hepatic carnitine palmitoyltransferase (CPT) by phospholipids. 1994 Biochem. Soc. Trans. pmid:7958184
Zammit VA et al. Structure-function relationships of the liver and muscle isoforms of carnitine palmitoyltransferase I. 2001 Biochem. Soc. Trans. pmid:11356169
Hegardt FG et al. Post-transcriptional regulation of rat carnitine octanoyltransferase. 2001 Biochem. Soc. Trans. pmid:11356174
McGarry JD Malonyl-CoA and carnitine palmitoyltransferase I: an expanding partnership. 1995 Biochem. Soc. Trans. pmid:8566378
Broadway NM and Saggerson ED Microsomal carnitine acyltransferases. 1995 Biochem. Soc. Trans. pmid:8566389
Fraser F et al. Evidence that both the acyl-CoA- and malonyl-CoA binding sites of mitochondrial overt carnitine palmitoyltransferase (CPT I) are exposed on the cytosolic face of the outer membrane. 1996 Biochem. Soc. Trans. pmid:8736842
Lane MD et al. Role of malonyl-CoA in the hypothalamic control of food intake and energy expenditure. 2005 Biochem. Soc. Trans. pmid:16246046
Ruderman NB et al. Malonyl-CoA and AMP-activated protein kinase (AMPK): possible links between insulin resistance in muscle and early endothelial cell damage in diabetes. 2003 Biochem. Soc. Trans. pmid:12546685
Hopkins TA et al. AMP-activated protein kinase regulation of fatty acid oxidation in the ischaemic heart. 2003 Biochem. Soc. Trans. pmid:12546686
Bergseth S et al. Is carnitine palmitoyltransferase inhibited by a malonyl-CoA-binding unit in the mitochondria? 1986 Biochem. Soc. Trans. pmid:3743880
Frayn KN The glucose-fatty acid cycle: a physiological perspective. 2003 Biochem. Soc. Trans. pmid:14641007
Carreras CW and Khosla C Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. 1998 Biochemistry pmid:9518007
Martinez MA et al. A novel role of malonyl-ACP in lipid homeostasis. 2010 Biochemistry pmid:20201588
Shi J et al. Deletion of the conserved first 18 N-terminal amino acid residues in rat liver carnitine palmitoyltransferase I abolishes malonyl-CoA sensitivity and binding. 1998 Biochemistry pmid:9692998
Rangan VS et al. Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro. 2001 Biochemistry pmid:11535054
Reeves CD et al. Alteration of the substrate specificity of a modular polyketide synthase acyltransferase domain through site-specific mutations. 2001 Biochemistry pmid:11747421
Kerner J and Bieber L Isolation of a malonyl-CoA-sensitive CPT/beta-oxidation enzyme complex from heart mitochondria. 1990 Biochemistry pmid:2350540
Nicot C et al. Pig liver carnitine palmitoyltransferase I, with low Km for carnitine and high sensitivity to malonyl-CoA inhibition, is a natural chimera of rat liver and muscle enzymes. 2001 Biochemistry pmid:11329295
Florova G et al. Enzymes involved in fatty acid and polyketide biosynthesis in Streptomyces glaucescens: role of FabH and FabD and their acyl carrier protein specificity. 2002 Biochemistry pmid:12173933
Zheng X et al. Substrate binding induces a cooperative conformational change in the 12S subunit of transcarboxylase: Raman crystallographic evidence. 2002 Biochemistry pmid:12196011
Witkowski A et al. Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase. 2002 Biochemistry pmid:12196027
Child CJ et al. Structural similarities between 6-methylsalicylic acid synthase from Penicillium patulum and vertebrate type I fatty acid synthase: evidence from thiol modification studies. 1996 Biochemistry pmid:8823160
Suzuki H et al. Proposed mechanism and functional amino acid residues of malonyl-CoA:anthocyanin 5-O-glucoside-6'''-O-malonyltransferase from flowers of Salvia splendens, a member of the versatile plant acyltransferase family. 2003 Biochemistry pmid:12578391
Prigge ST et al. The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII. 2003 Biochemistry pmid:12549938
Liou GF et al. Quantitative analysis of loading and extender acyltransferases of modular polyketide synthases. 2003 Biochemistry pmid:12515555
Shi J et al. The first 28 N-terminal amino acid residues of human heart muscle carnitine palmitoyltransferase I are essential for malonyl CoA sensitivity and high-affinity binding. 2000 Biochemistry pmid:10651636
Jez JM et al. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. 2000 Biochemistry pmid:10653632
Kumar S and Srinivasan KR Inactivation of chicken liver fatty acid synthetase by malonyl coenzyme A. Effects of acetyl coenzyme A and nicotinamide adenine dinucleotide phosphate. 1981 Biochemistry pmid:7260044
Srinivasan KR and Kumar S Kinetic analysis of the malonyl coenzyme A decarboxylation and the condensation reaction of fatty acid synthesis. Application to the study of malonyl coenzyme A inactivated chicken liver fatty acid synthetase. 1981 Biochemistry pmid:7260045
Fujii I et al. Enzymatic synthesis of 1,3,6,8-tetrahydroxynaphthalene solely from malonyl coenzyme A by a fungal iterative type I polyketide synthase PKS1. 2000 Biochemistry pmid:10913297
Anderson VE and Hammes GG Distribution of reaction intermediates on chicken liver fatty acid synthase. 1985 Biochemistry pmid:3995008
Mazur MT et al. Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by fourier transform mass spectrometry: the polyketide module of yersiniabactin synthetase. 2003 Biochemistry pmid:14621984
Tseng CC et al. Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase. 2004 Biochemistry pmid:14744141
Spencer JB and Jordan PM Investigation of the mechanism and steric course of the reaction catalyzed by 6-methylsalicylic acid synthase from Penicillium patulum using (R)-[1-13C;2-2H]- and (S)-[1-13C;2-2H]malonates. 1992 Biochemistry pmid:1390697
Relat J et al. Pig muscle carnitine palmitoyltransferase I (CPTI beta), with low Km for carnitine and low sensitivity to malonyl-CoA inhibition, has kinetic characteristics similar to those of the rat liver (CPTI alpha) enzyme. 2004 Biochemistry pmid:15449958
Chung CH et al. Conferral of malonyl coenzyme A sensitivity to purified rat heart mitochondrial carnitine palmitoyltransferase. 1992 Biochemistry pmid:1390753
Preisig-Müller R et al. Plant polyketide synthases leading to stilbenoids have a domain catalyzing malonyl-CoA:CO2 exchange, malonyl-CoA decarboxylation, and covalent enzyme modification and a site for chain lengthening. 1997 Biochemistry pmid:9204882
de Vries Y et al. Functional characterization of mitochondrial carnitine palmitoyltransferases I and II expressed in the yeast Pichia pastoris. 1997 Biochemistry pmid:9136891
Dunn BJ et al. Comparative analysis of the substrate specificity of trans- versus cis-acyltransferases of assembly line polyketide synthases. 2014 Biochemistry pmid:24871074
Buttke TM and Ingram LO Inhibition of unsaturated fatty acid synthesis in escherichia coli by the antibiotic cerulenin. 1978 Biochemistry pmid:365224
Kashfi K et al. Hepatic carnitine palmitoyltransferase-I has two independent inhibitory binding sites for regulation of fatty acid oxidation. 1994 Biochim. Biophys. Acta pmid:8180250
Guzmán M and Castro J Ethanol increases the sensitivity of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in short-term hepatocyte incubations. 1989 Biochim. Biophys. Acta pmid:2713390
Skrede S and Bremer J Acylcarnitine formation and fatty acid oxidation in hepatocytes from rats treated with tetradecylthioacetic acid (a 3-thia fatty acid). 1993 Biochim. Biophys. Acta pmid:8466948
Bergseth S et al. Carnitine palmitoyltransferase: activation and inactivation in liver mitochondria from fed, fasted, hypo- and hyperthyroid rats. 1986 Biochim. Biophys. Acta pmid:3707984
Lund H et al. Effects of thyroid state and fasting on the concentrations of CoA and malonyl-CoA in rat liver. 1986 Biochim. Biophys. Acta pmid:3707992
Lund H Carnitine palmitoyltransferase: characterization of a labile detergent-extracted malonyl-CoA-sensitive enzyme from rat liver mitochondria. 1987 Biochim. Biophys. Acta pmid:3828368
Bhatia H et al. miR-107 orchestrates ER stress induction and lipid accumulation by post-transcriptional regulation of fatty acid synthase in hepatocytes. 2014 Biochim. Biophys. Acta pmid:24560669
McGarry JD et al. Characteristics of fatty acid oxidation in rat liver homogenates and the inhibitory effect of malonyl-CoA. 1978 Biochim. Biophys. Acta pmid:698234